Iron in PDB 3ua5: Crystal Structure of P450 2B6 (Y226H/K262R) in Complex with Two Molecules of Amlodipine

All present enzymatic activity of Crystal Structure of P450 2B6 (Y226H/K262R) in Complex with Two Molecules of Amlodipine:
1.14.14.1;

The structure of Crystal Structure of P450 2B6 (Y226H/K262R) in Complex with Two Molecules of Amlodipine, PDB code: 3ua5 was solved by M.B.Shah, C.D.Stout, J.R.Halpert, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	82.45 / 2.80
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	58.000, 78.300, 247.340, 90.00, 90.00, 90.00
R / Rfree (%)	24.2 / 29.4

The structure of Crystal Structure of P450 2B6 (Y226H/K262R) in Complex with Two Molecules of Amlodipine also contains other interesting chemical elements:

Chlorine

(Cl)

4 atoms

The binding sites of Iron atom in the Crystal Structure of P450 2B6 (Y226H/K262R) in Complex with Two Molecules of Amlodipine (pdb code 3ua5). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Crystal Structure of P450 2B6 (Y226H/K262R) in Complex with Two Molecules of Amlodipine, PDB code: 3ua5:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Crystal Structure of P450 2B6 (Y226H/K262R) in Complex with Two Molecules of Amlodipine


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Crystal Structure of P450 2B6 (Y226H/K262R) in Complex with Two Molecules of Amlodipine within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe500 b:40.4 occ:1.00 FE A:HEM500 0.0 40.4 1.0 NA A:HEM500 1.7 39.3 1.0 NB A:HEM500 1.8 39.5 1.0 NC A:HEM500 1.9 41.2 1.0 ND A:HEM500 1.9 40.6 1.0 NAD A:06X501 2.2 32.7 1.0 SG A:CYS436 2.6 20.0 1.0 C4A A:HEM500 2.7 39.0 1.0 C1A A:HEM500 2.7 39.4 1.0 C1B A:HEM500 2.8 38.6 1.0 C4B A:HEM500 2.9 39.0 1.0 C4D A:HEM500 2.9 40.7 1.0 C4C A:HEM500 3.0 43.6 1.0 C1D A:HEM500 3.0 41.5 1.0 C1C A:HEM500 3.0 42.0 1.0 CHB A:HEM500 3.2 38.6 1.0 CHA A:HEM500 3.3 39.7 1.0 CB A:CYS436 3.4 20.0 1.0 CHD A:HEM500 3.4 42.8 1.0 CHC A:HEM500 3.4 41.2 1.0 CAM A:06X501 3.6 35.1 1.0 C3A A:HEM500 3.9 39.1 1.0 C2A A:HEM500 3.9 38.5 1.0 CA A:CYS436 4.0 30.0 1.0 C2B A:HEM500 4.0 38.3 1.0 C3B A:HEM500 4.1 39.4 1.0 C3D A:HEM500 4.2 41.4 1.0 C2D A:HEM500 4.2 42.0 1.0 C3C A:HEM500 4.2 44.3 1.0 C2C A:HEM500 4.2 43.2 1.0 N A:LEU437 4.5 37.4 1.0 C A:CYS436 4.6 30.0 1.0 CAN A:06X501 4.7 33.9 1.0 N A:GLY438 4.7 39.6 1.0 O A:ALA298 5.0 46.0 1.0

Iron binding site 2 out of 2 in the Crystal Structure of P450 2B6 (Y226H/K262R) in Complex with Two Molecules of Amlodipine


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Crystal Structure of P450 2B6 (Y226H/K262R) in Complex with Two Molecules of Amlodipine within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe500 b:38.1 occ:1.00 FE B:HEM500 0.0 38.1 1.0 NC B:HEM500 1.7 36.7 1.0 NB B:HEM500 1.8 36.4 1.0 ND B:HEM500 1.8 37.4 1.0 NA B:HEM500 1.9 37.3 1.0 NAD B:06X501 2.2 48.8 1.0 SG B:CYS436 2.4 28.0 1.0 C1C B:HEM500 2.8 38.1 1.0 C4B B:HEM500 2.8 38.5 1.0 C4C B:HEM500 2.8 36.9 1.0 C4D B:HEM500 2.8 37.6 1.0 C1B B:HEM500 2.9 37.4 1.0 C1D B:HEM500 2.9 38.1 1.0 C1A B:HEM500 2.9 38.0 1.0 C4A B:HEM500 3.0 37.0 1.0 CHC B:HEM500 3.2 38.7 1.0 CHA B:HEM500 3.3 37.8 1.0 CB B:CYS436 3.3 34.0 1.0 CHD B:HEM500 3.3 37.6 1.0 CHB B:HEM500 3.4 36.9 1.0 CAM B:06X501 3.6 50.1 1.0 C2C B:HEM500 4.0 37.9 1.0 C3C B:HEM500 4.0 37.3 1.0 C3B B:HEM500 4.0 39.6 1.0 C2B B:HEM500 4.1 38.2 1.0 C3D B:HEM500 4.1 38.0 1.0 CA B:CYS436 4.1 34.7 1.0 C2D B:HEM500 4.1 38.3 1.0 C2A B:HEM500 4.1 38.1 1.0 C3A B:HEM500 4.2 37.5 1.0 N B:LEU437 4.6 37.4 1.0 CAN B:06X501 4.6 49.0 1.0 C B:CYS436 4.7 36.4 1.0 N B:GLY438 4.8 39.3 1.0 CD1 B:PHE429 4.9 33.2 1.0 O B:ALA298 5.0 45.7 1.0

M.B.Shah, P.R.Wilderman, J.Pascual, Q.Zhang, C.D.Stout, J.R.Halpert. Conformational Adaptation of Human Cytochrome P450 2B6 and Rabbit Cytochrome P450 2B4 Revealed Upon Binding Multiple Amlodipine Molecules. Biochemistry V. 51 7225 2012.
ISSN: ISSN 0006-2960
PubMed: 22909231
DOI: 10.1021/BI300894Z